Structure of the mechanosensitive Piezo1 channel. Determined by electron microscopy at 3.97 Å resolution. Released 31 Jan 2018.
Explore 5Z10 in 3D Show helices and sheets RCSB PDB PDBe
5Z10 contains 168 α-helices and 54 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 578-584 | 7 | |
| α-helix | 587-595 | 9 | |
| α-helix | 608-623 | 16 | |
| α-helix | 632-649 | 18 | |
| α-helix | 693-702 | 10 | |
| α-helix | 703-707 | 5 | |
| α-helix | 710-713 | 4 | |
| α-helix | 786-820 | 35 | |
| α-helix | 829-839 | 11 | |
| α-helix | 846-865 | 20 | |
| α-helix | 922-949 | 28 | |
| β-strand | 971 | 1 | 1 |
| β-strand | 973 | 1 | 1 |
| α-helix | 974-982 | 9 | |
| α-helix | 990-1005 | 16 | |
| α-helix | 1008-1022 | 15 | |
| α-helix | 1028-1052 | 25 | |
| α-helix | 1092-1110 | 19 | |
| α-helix | 1142-1144 | 3 | |
| α-helix | 1151-1158 | 8 | |
| α-helix | 1164-1172 | 9 | |
| α-helix | 1182-1198 | 17 | |
| α-helix | 1203-1223 | 21 | |
| α-helix | 1280-1298 | 19 | |
| α-helix | 1303-1314 | 12 | |
| α-helix | 1316-1361 | 46 | |
| α-helix | 1412-1414 | 3 | |
| α-helix | 1505-1544 | 40 | |
| α-helix | 1657-1668 | 12 | |
| α-helix | 1673-1685 | 13 | |
| α-helix | 1689-1700 | 12 | |
| α-helix | 1706-1708 | 3 | |
| α-helix | 1709-1713 | 5 | |
| α-helix | 1714-1718 | 5 | |
| α-helix | 1729-1742 | 14 | |
| α-helix | 1781-1800 | 20 | |
| α-helix | 1959-1965 | 7 | |
| α-helix | 1980-1993 | 14 | |
| α-helix | 2016-2039 | 24 | |
| α-helix | 2044-2060 | 17 | |
| α-helix | 2077-2099 | 23 | |
| α-helix | 2116-2125 | 10 | |
| α-helix | 2132-2142 | 11 | |
| α-helix | 2150-2173 | 24 | |
| α-helix | 2185-2204 | 20 | |
| α-helix | 2205-2207 | 3 | |
| β-strand | 2225-2232 | 8 | 2 |
| β-strand | 2239-2243 | 5 | 2 |
| β-strand | 2248-2250 | 3 | 3 |
| α-helix | 2251-2252 | 2 | |
| α-helix | 2253-2261 | 9 | |
| α-helix | 2267-2275 | 9 | |
| α-helix | 2278-2280 | 3 | |
| β-strand | 2281-2287 | 7 | 3 |
| α-helix | 2298-2310 | 13 | |
| β-strand | 2315-2324 | 10 | 2 |
| β-strand | 2335-2344 | 10 | 2 |
| α-helix | 2349-2357 | 9 | |
| β-strand | 2372 | 1 | 4 |
| β-strand | 2375-2377 | 3 | 3 |
| β-strand | 2383 | 1 | 2 |
| β-strand | 2385-2386 | 2 | 3 |
| β-strand | 2399 | 1 | 4 |
| β-strand | 2401-2406 | 6 | 5 |
| β-strand | 2409 | 1 | 6 |
| α-helix | 2421-2425 | 5 | |
| β-strand | 2426 | 1 | 6 |
| β-strand | 2429-2434 | 6 | 5 |
| β-strand | 2443-2449 | 7 | 3 |
| α-helix | 2467-2481 | 15 | |
| α-helix | 2501-2516 | 16 | |
| α-helix | 2519-2521 | 3 | |
| α-helix | 2526-2534 | 9 | |
| α-helix | 2537-2540 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Piezo-type mechanosensitive ion channel component 1 | A, B, C | protein | 2547 | Mus musculus | E2JF22 (AlphaFold model) |
>5Z10_1 Piezo-type mechanosensitive ion channel component 1 (chains A, B, C) MEPHVLGAGLYWLLLPCTLLAASLLRFNALSLVYLLFLLLLPWLPGPSRHSIPGHTGRLL RALLCLSLLFLVAHLAFQICLHTVPHLDQFLGQNGSLWVKVSQHIGVTRLDLKDIFNTTR LVAPDLGVLLASSLCLGLCGRLTRKAGQSRRTQELQDDDDDDDDDDEDIDAAPAVGLKGA PALATKRRLWLASRFRVTAHWLLMTSGRTLVIVLLALAGIAHPSAFSSIYLVVFLAICTW WSCHFPLSPLGFNTLCVMVSCFGAGHLICLYCYQTPFIQDMLPPGNIWARLFGLKNFVDL PNYSSPNALVLNTKHAWPIYVSPGILLLLYYTATSLLKLHKSCPSELRKETPREDEEHEL ELDHLEPEPQARDATQGEMPMTTEPDLDNCTVHVLTSQSPVRQRPVRPRLAELKEMSPLH GLGHLIMDQSYVCALIAMMVWSIMYHSWLTFVLLLWACLIWTVRSRHQLAMLCSPCILLY GLTLCCLRYVWAMELPELPTTLGPVSLHQLGLEHTRYPCLDLGAMLLYLLTFWLLLRQFV KEKLLKKQKVPAALLEVTVADTEPTQTQTLLRSLGELVTGIYVKYWIYVCAGMFIVVSFA GRLVVYKIVYMFLFLLCLTLFQVYYTLWRKLLRVFWWLVVAYTMLVLIAVYTFQFQDFPT YWRNLTGFTDEQLGDLGLEQFSVSELFSSILIPGFFLLACILQLHYFHRPFMQLTDLEHV PPPGTRHPRWAHRQDAVSEAPLLEHQEEEEVFREDGQSMDGPHQATQVPEGTASKWGLVA DRLLDLAASFSAVLTRIQVFVRRLLELHVFKLVALYTVWVALKEVSVMNLLLVVLWAFAL PYPRFRPMASCLSTVWTCIIIVCKMLYQLKIVNPHEYSSNCTEPFPNNTNLQPLEINQSL LYRGPVDPANWFGVRKGYPNLGYIQNHLQILLLLVFEAVVYRRQEHYRRQHQQAPLPAQA VCADGTRQRLDQDLLSCLKYFINFFFYKFGLEICFLMAVNVIGQRMNFMVILHGCWLVAI LTRRRREAIARLWPNYCLFLTLFLLYQYLLCLGMPPALCIDYPWRWSKAIPMNSALIKWL YLPDFFRAPNSTNLISDFLLLLCASQQWQVFSAERTEEWQRMAGINTDHLEPLRGEPNPI PNFIHCRSYLDMLKVAVFRYLFWLVLVVVFVAGATRISIFGLGYLLACFYLLLFGTTLLQ KDTRAQLVLWDCLILYNVTVIISKNMLSLLSCVFVEQMQSNFCWVIQLFSLVCTVKGYYD PKEMMTRDRDCLLPVEEAGIIWDSICFFFLLLQRRIFLSHYFLHVSADLKATALQASRGF ALYNAANLKSINFHRQIEEKSLAQLKRQMKRIRAKQEKYRQSQASRGQLQSKDPQDPSQE PGPDSPGGSSPPRRQWWRPWLDHATVIHSGDYFLFESDSEEEEEALPEDPRPAAQSAFQM AYQAWVTNAQTVLRQRRERARQERAEQLASGGDLNPDVEPVDVPEDEMAGRSHMMQRVLS TMQFLWVLGQATVDGLTRWLRAFTKHHRTMSDVLCAERYLLTQELLRVGEVRRGVLDQLY VGEDEATLSGPVETRDGPSTASSGLGAEEPLSSMTDDTSSPLSTGYNTRSGSEEIVTDAG DLQAGTSLHGSQELLANARTRMRTASELLLDRRLHIPELEEAERFEAQQGRTLRLLRAGY QCVAAHSELLCYFIIILNHMVTASAASLVLPVLVFLWAMLTIPRPSKRFWMTAIVFTEVM VVTKYLFQFGFFPWNSYVVLRRYENKPYFPPRILGLEKTDSYIKYDLVQLMALFFHRSQL LCYGLWDHEEDRYPKDHCRSSVKDREAKEEPEAKLESQSETGTGHPKEPVLAGTPRDHIQ GKGSIRSKDVIQDPPEDLKPRHTRHISIRFRRRKETPGPKGTAVMETEHEEGEGKETTER KRPRHTQEKSKFRERMKAAGRRLQSFCVSLAQSFYQPLQRFFHDILHTKYRAATDVYALM FLADIVDIIIIIFGFWAFGKHSAATDIASSLSDDQVPQAFLFMLLVQFGTMVIDRALYLR KTVLGKLAFQVVLVVAIHIWMFFILPAVTERMFSQNAVAQLWYFVKCIYFALSAYQIRCG YPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSNWMCVEDIYA NIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLIRSVVGVV NQPIDVTVTLKLGGYEPLFTMSAQQPSIVPFTPQAYEELSQQFDPYPLAMQFISQYSPED IVTAQIEGSSGALWRISPPSRAQMKQELYNGTADITLRFTWNFQRDLAKGGTVEYTNEKH TLELAPNSTARRQLAQLLEGRPDQSVVIPHLFPKYIRAPNGPEANPVKQLQPDEEEDYLG VRIQLRREQVGTGASGEQAGTKASDFLEWWVIELQDCKADCNLLPMVIFSDKVSPPSLGF LAGYGIVGLYVSIVLVVGKFVRGFFSEISHSIMFEELPCVDRILKLCQDIFLVRETRELE LEEELYAKLIFLYRSPETMIKWTRERE
Structure and mechanogating mechanism of the Piezo1 channel. Zhao, Q., Zhou, H., Chi, S. et al. Nature (2018) 554:487-492. DOI 10.1038/nature25743 · PubMed
Other PDB entries of the same protein (UniProt E2JF22 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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